General Information

    • DRAMP ID

    • DRAMP02436

    • Peptide Name

    • Chitinase

    • Source

    • Streptomyces violaceus (Streptomyces venezuelae)

    • Family

    • Belongs to the glycosyl hydrolase 18 family Chitinase (class

    • Gene

    • Not found

    • Sequence

    • EQPGGDKVNLGYFTN

    • Sequence Length

    • 15

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antifungal

    • Target Organism

      • Fungi: Aspergillus niger, Alternaria alternata, Hordeum sativum.

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Chitin-binding

Structure Information

    • Linear/Cyclic

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet

    • Stereochemistry

    • Not included yet

    • Structure

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP02436 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP02436.

Physicochemical Information

    • Formula

    • C72H107N19O25

    • Absent Amino Acids

    • ACHIMRSW

    • Common Amino Acids

    • G

    • Mass

    • 1638.75

    • PI

    • 4.37

    • Basic Residues

    • 1

    • Acidic Residues

    • 2

    • Hydrophobic Residues

    • 3

    • Net Charge

    • -1

    • Boman Index

    • -27.85

    • Hydrophobicity

    • -1.027

    • Aliphatic Index

    • 45.33

    • Half Life

      • Mammalian:1 hour
      • Yeast:30 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 1490

    • Absorbance 280nm

    • 106.43

    • Polar Residues

    • 7

DRAMP02436

Comments Information

    • Function

    • Has antifungal activity.

    • Catalytic activity

    • Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

    • Enzyme regulation

    • Inhibited by divalent metal ions. Maximum inhibition observed with Ca2+ while the least inhibition was observed with Fe2+. Inhibited by high concentrations of GlcNAc.

    • Biophysicochemical properties

    • pH dependence (Optimum pH is 6-8. There is a 37.7% decrease in activity at pH 5 and a 39.8% decrease in activity at pH 9); Temperature dependence (Optimum temperature is 35 degrees Celsius).

Literature Information

  • ·Literature 1

    • Title

    • Extracellular production of chitinase by Streptomyces venezuelae.

    • Reference

    • Thesis (2005), Visva Bharati (Central University), India.

    • Author

    • Mukherjee G.
  • ·Literature 2

    • Title

    • Purification, characterization, and antifungal activity of chitinase from Streptomyces venezuelae P(10).

    • Reference

    • Curr Microbiol. 2006 Oct;53(4):265-269.

    • Author

    • Mukherjee G, Sen SK.